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Literature summary extracted from

  • Kim, H.T.; Ko, H.J.; Kim, N.; Kim, D.; Lee, D.; Choi, I.G.; Woo, H.C.; Kim, M.D.; Kim, K.H.
    Characterization of a recombinant endo-type alginate lyase (Alg7D) from Saccharophagus degradans (2012), Biotechnol. Lett., 34, 1087-1092.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.2.3 gene alg7D, overexpression of soluble His-tagged enzyme lacking the signal peptide in Escherichia coli strain BL21(DE3) Saccharophagus degradans
4.2.2.11 gene alg7D, overexpression of soluble His-tagged enzyme lacking the signal peptide in Escherichia coli strain BL21(DE3) Saccharophagus degradans

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.2.3 Ca2+
-
Saccharophagus degradans
4.2.2.3 Cu2+
-
Saccharophagus degradans
4.2.2.3 Fe2+
-
Saccharophagus degradans
4.2.2.3 Mg2+
-
Saccharophagus degradans
4.2.2.3 Mn2+
-
Saccharophagus degradans
4.2.2.3 Zn2+
-
Saccharophagus degradans
4.2.2.11 Ca2+
-
Saccharophagus degradans
4.2.2.11 Cu2+
-
Saccharophagus degradans
4.2.2.11 Fe2+
-
Saccharophagus degradans
4.2.2.11 Mg2+
-
Saccharophagus degradans
4.2.2.11 Mn2+
-
Saccharophagus degradans
4.2.2.11 Zn2+
-
Saccharophagus degradans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.2.3 additional information
-
additional information kinetics, overview Saccharophagus degradans
4.2.2.11 additional information
-
additional information kinetics, overview Saccharophagus degradans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.2.3 additional information no effect on activity by K+ Saccharophagus degradans
4.2.2.3 Na+ slight activation Saccharophagus degradans
4.2.2.11 additional information no effect on activity by K+ Saccharophagus degradans
4.2.2.11 Na+ slight activation Saccharophagus degradans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.2.3 32700
-
x * 32700, recombinant His-tagged enzyme without, SDS-PAGE Saccharophagus degradans
4.2.2.11 32700
-
x * 32700, recombinant His-tagged enzyme without, SDS-PAGE Saccharophagus degradans

Organism

EC Number Organism UniProt Comment Textmining
4.2.2.3 Saccharophagus degradans
-
gene alg7D
-
4.2.2.11 Saccharophagus degradans
-
gene alg7D
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.2.3 recombinant His-tagged enzyme lacking the signal peptide from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration Saccharophagus degradans
4.2.2.11 recombinant His-tagged enzyme lacking the signal peptide from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration Saccharophagus degradans

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.2.2.3 1.98
-
wild-type enzyme, pH 7.0, 50°C, substrate alginate Saccharophagus degradans
4.2.2.3 41.4
-
purified recombinant His-tagged enzyme, pH 7.0, 50°C, substrate alginate Saccharophagus degradans
4.2.2.3 67
-
purified recombinant His-tagged enzyme, substrate poly(beta-D-mannuronate), pH 7.0, 50°C Saccharophagus degradans
4.2.2.11 1.98
-
wild-type enzyme, pH 7.0, 50°C, substrate alginate Saccharophagus degradans
4.2.2.11 41.4
-
purified recombinant His-tagged enzyme, pH 7.0, 50°C, substrate alginate Saccharophagus degradans
4.2.2.11 46
-
purified recombinant His-tagged enzyme, substrate poly(alpha-L-guluronate), pH 7.0, 50°C Saccharophagus degradans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.2.3 alginate the enzyme endolytically depolymerizes alginate by beta-elimination into oligo-alginates with degrees of polymerization of 2-5 Saccharophagus degradans ?
-
?
4.2.2.3 additional information the enzyme is active on poly(beta-D-mannuronate) and poly(alpha-L-guluronate), cf. EC 4.2.2.11 Saccharophagus degradans ?
-
?
4.2.2.3 poly(beta-D-mannuronate)
-
Saccharophagus degradans ?
-
?
4.2.2.11 alginate the enzyme endolytically depolymerizes alginate by beta-elimination into oligo-alginates with degrees of polymerization of 2-5 Saccharophagus degradans ?
-
?
4.2.2.11 additional information the enzyme is active on poly(alpha-L-guluronate) and poly(beta-D-mannuronate), cf. EC 4.2.2.3 Saccharophagus degradans ?
-
?
4.2.2.11 poly(alpha-L-guluronate)
-
Saccharophagus degradans ?
-
?

Subunits

EC Number Subunits Comment Organism
4.2.2.3 ? x * 32700, recombinant His-tagged enzyme without, SDS-PAGE Saccharophagus degradans
4.2.2.11 ? x * 32700, recombinant His-tagged enzyme without, SDS-PAGE Saccharophagus degradans

Synonyms

EC Number Synonyms Comment Organism
4.2.2.3 Alg7D
-
Saccharophagus degradans
4.2.2.3 alginate lyase
-
Saccharophagus degradans
4.2.2.3 endo-type alginate lyase
-
Saccharophagus degradans
4.2.2.11 Alg7D
-
Saccharophagus degradans
4.2.2.11 alginate lyase
-
Saccharophagus degradans
4.2.2.11 endo-type alginate lyase
-
Saccharophagus degradans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.2.3 50
-
recombinant enzyme Saccharophagus degradans
4.2.2.11 50
-
recombinant enzyme Saccharophagus degradans

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
4.2.2.3 20 70 activity range, profile overview Saccharophagus degradans
4.2.2.11 20 70 activity range, profile overview Saccharophagus degradans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.2.3 7
-
recombinant enzyme Saccharophagus degradans
4.2.2.11 7
-
recombinant enzyme Saccharophagus degradans

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.2.2.3 5 11 activity range, profile overview Saccharophagus degradans
4.2.2.11 5 11 activity range, profile overview Saccharophagus degradans

General Information

EC Number General Information Comment Organism
4.2.2.3 evolution the enzyme belongs to the to the polysaccharide lyase-7 family Saccharophagus degradans
4.2.2.11 evolution the enzyme belongs to the to the polysaccharide lyase-7 family Saccharophagus degradans